Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Peptidyl-prolyl cis-trans isomerase FKBP1A

Gene

Fkbp1a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. Recruites SMAD7 to ACVR1B which prevents the association of SMAD2 and SMAD3 with the activin receptor complex, thereby blocking the activin signal. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).By similarity

Catalytic activityi

Peptidylproline (omega=180) = peptidylproline (omega=0).

Enzyme regulationi

Inhibited by both FK506 and rapamycin.

GO - Molecular functioni

  • activin binding Source: MGI
  • calcium channel inhibitor activity Source: GO_Central
  • drug binding Source: MGI
  • FK506 binding Source: MGI
  • ion channel binding Source: BHF-UCL
  • peptidyl-prolyl cis-trans isomerase activity Source: MGI
  • protein homodimerization activity Source: MGI
  • signal transducer activity Source: MGI
  • SMAD binding Source: MGI

GO - Biological processi

  • amyloid fibril formation Source: MGI
  • chaperone-mediated protein folding Source: GO_Central
  • cytokine-mediated signaling pathway Source: MGI
  • extracellular fibril organization Source: MGI
  • heart morphogenesis Source: BHF-UCL
  • heart trabecula formation Source: BHF-UCL
  • muscle contraction Source: MGI
  • negative regulation of protein phosphatase type 2B activity Source: MGI
  • negative regulation of protein phosphorylation Source: MGI
  • negative regulation of release of sequestered calcium ion into cytosol Source: GO_Central
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: MGI
  • positive regulation of protein binding Source: MGI
  • positive regulation of protein ubiquitination Source: MGI
  • protein peptidyl-prolyl isomerization Source: MGI
  • regulation of activin receptor signaling pathway Source: MGI
  • regulation of amyloid precursor protein catabolic process Source: MGI
  • regulation of immune response Source: MGI
  • regulation of protein localization Source: MGI
  • regulation of ryanodine-sensitive calcium-release channel activity Source: BHF-UCL
  • release of sequestered calcium ion into cytosol Source: MGI
  • response to caffeine Source: MGI
  • response to iron ion Source: Ensembl
  • SMAD protein complex assembly Source: MGI
  • T cell proliferation Source: MGI
  • ventricular cardiac muscle tissue morphogenesis Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Isomerase, Rotamase

Enzyme and pathway databases

ReactomeiREACT_294284. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
REACT_297798. TGF-beta receptor signaling activates SMADs.

Names & Taxonomyi

Protein namesi
Recommended name:
Peptidyl-prolyl cis-trans isomerase FKBP1A (EC:5.2.1.8)
Short name:
PPIase FKBP1A
Alternative name(s):
12 kDa FK506-binding protein
Short name:
12 kDa FKBP
Short name:
FKBP-12
Calstabin-1
FK506-binding protein 1A
Short name:
FKBP-1A
Immunophilin FKBP12
Rotamase
Gene namesi
Name:Fkbp1a
Synonyms:Fkbp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:95541. Fkbp1a.

Subcellular locationi

GO - Cellular componenti

  • axon terminus Source: Ensembl
  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • extracellular exosome Source: MGI
  • extracellular matrix Source: GOC
  • membrane Source: MGI
  • sarcoplasmic reticulum membrane Source: MGI
  • Z disc Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 108107Peptidyl-prolyl cis-trans isomerase FKBP1APRO_0000075290Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 531N6-acetyllysine; alternate1 Publication
Modified residuei53 – 531N6-succinyllysine; alternate1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP26883.
PaxDbiP26883.
PRIDEiP26883.

PTM databases

PhosphoSiteiP26883.

Expressioni

Gene expression databases

BgeeiP26883.
CleanExiMM_FKBP1A.
ExpressionAtlasiP26883. baseline and differential.
GenevisibleiP26883. MM.

Interactioni

Subunit structurei

Interacts with TGFBR1; prevents TGFBR1 phosphorylation by TGFBR2 and stabilizes it in the inactive conformation (By similarity). Interacts with ACVR1B and SMAD7. Interacts directly with RYR1, RYR2 and RYR3 (By similarity). Identified in a complex composed of RYR1, PDE4D, PKA, FKBP1A and protein phosphatase 1 (PP1).By similarity1 Publication

Protein-protein interaction databases

BioGridi199682. 3 interactions.
DIPiDIP-29707N.
IntActiP26883. 3 interactions.
MINTiMINT-4095099.
STRINGi10090.ENSMUSP00000037206.

Structurei

3D structure databases

ProteinModelPortaliP26883.
SMRiP26883. Positions 2-108.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini20 – 10889PPIase FKBP-typePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PPIase FKBP-type domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0545.
GeneTreeiENSGT00760000119159.
HOGENOMiHOG000154887.
HOVERGENiHBG051623.
InParanoidiP26883.
KOiK09568.
OMAiTIPGPYA.
OrthoDBiEOG7ZGX5T.
TreeFamiTF105291.

Family and domain databases

InterProiIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERiPTHR10516. PTHR10516. 1 hit.
PfamiPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEiPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P26883-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGVQVETISP GDGRTFPKRG QTCVVHYTGM LEDGKKFDSS RDRNKPFKFT
60 70 80 90 100
LGKQEVIRGW EEGVAQMSVG QRAKLIISSD YAYGATGHPG IIPPHATLVF

DVELLKLE
Length:108
Mass (Da):11,923
Last modified:January 23, 2007 - v2
Checksum:i8C265ED5803F6987
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60203 mRNA. Translation: CAA42762.1.
U65100, U65098, U65099 Genomic DNA. Translation: AAB17554.1.
AF483488 mRNA. Translation: AAL90762.1.
AF483489 mRNA. Translation: AAL90763.1.
AK002777 mRNA. Translation: BAB22351.1.
AK010693 mRNA. Translation: BAB27125.1.
AK019362 mRNA. Translation: BAB31680.1.
AK154751 mRNA. Translation: BAE32804.1.
AK168333 mRNA. Translation: BAE40271.1.
AK169186 mRNA. Translation: BAE40963.1.
AK169242 mRNA. Translation: BAE41008.1.
BC004671 mRNA. Translation: AAH04671.1.
CCDSiCCDS16869.1.
PIRiJH0528.
RefSeqiNP_001289006.1. NM_001302077.1.
NP_001289007.1. NM_001302078.1.
NP_001289008.1. NM_001302079.1.
NP_001289009.1. NM_001302080.1.
NP_032045.1. NM_008019.3.
UniGeneiMm.278458.

Genome annotation databases

EnsembliENSMUST00000044011; ENSMUSP00000037206; ENSMUSG00000032966.
GeneIDi14225.
KEGGimmu:14225.
UCSCiuc008ndy.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60203 mRNA. Translation: CAA42762.1.
U65100, U65098, U65099 Genomic DNA. Translation: AAB17554.1.
AF483488 mRNA. Translation: AAL90762.1.
AF483489 mRNA. Translation: AAL90763.1.
AK002777 mRNA. Translation: BAB22351.1.
AK010693 mRNA. Translation: BAB27125.1.
AK019362 mRNA. Translation: BAB31680.1.
AK154751 mRNA. Translation: BAE32804.1.
AK168333 mRNA. Translation: BAE40271.1.
AK169186 mRNA. Translation: BAE40963.1.
AK169242 mRNA. Translation: BAE41008.1.
BC004671 mRNA. Translation: AAH04671.1.
CCDSiCCDS16869.1.
PIRiJH0528.
RefSeqiNP_001289006.1. NM_001302077.1.
NP_001289007.1. NM_001302078.1.
NP_001289008.1. NM_001302079.1.
NP_001289009.1. NM_001302080.1.
NP_032045.1. NM_008019.3.
UniGeneiMm.278458.

3D structure databases

ProteinModelPortaliP26883.
SMRiP26883. Positions 2-108.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199682. 3 interactions.
DIPiDIP-29707N.
IntActiP26883. 3 interactions.
MINTiMINT-4095099.
STRINGi10090.ENSMUSP00000037206.

PTM databases

PhosphoSiteiP26883.

Proteomic databases

MaxQBiP26883.
PaxDbiP26883.
PRIDEiP26883.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000044011; ENSMUSP00000037206; ENSMUSG00000032966.
GeneIDi14225.
KEGGimmu:14225.
UCSCiuc008ndy.1. mouse.

Organism-specific databases

CTDi2280.
MGIiMGI:95541. Fkbp1a.

Phylogenomic databases

eggNOGiCOG0545.
GeneTreeiENSGT00760000119159.
HOGENOMiHOG000154887.
HOVERGENiHBG051623.
InParanoidiP26883.
KOiK09568.
OMAiTIPGPYA.
OrthoDBiEOG7ZGX5T.
TreeFamiTF105291.

Enzyme and pathway databases

ReactomeiREACT_294284. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
REACT_297798. TGF-beta receptor signaling activates SMADs.

Miscellaneous databases

NextBioi285479.
PROiP26883.
SOURCEiSearch...

Gene expression databases

BgeeiP26883.
CleanExiMM_FKBP1A.
ExpressionAtlasiP26883. baseline and differential.
GenevisibleiP26883. MM.

Family and domain databases

InterProiIPR023566. PPIase_FKBP.
IPR001179. PPIase_FKBP_dom.
[Graphical view]
PANTHERiPTHR10516. PTHR10516. 1 hit.
PfamiPF00254. FKBP_C. 1 hit.
[Graphical view]
PROSITEiPS50059. FKBP_PPIASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA encoding murine FK506-binding protein (FKBP): nucleotide and deduced amino acid sequence."
    Nelson P.A., Lippke J.A., Murcko M.A., Rosborough S.L., Peattie D.A.
    Gene 109:255-258(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6 X CBA.
  2. Shou W., Bao S., Mathews L.S., Matzuk M.M.
    Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: 129/Sv.
  3. "High-throughput sequence identification of gene coding variants within alcohol-related QTLs."
    Ehringer M.A., Thompson J., Conroy O., Xu Y., Yang F., Canniff J., Beeson M., Gordon L., Bennett B., Johnson T.E., Sikela J.M.
    Mamm. Genome 12:657-663(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: ILS and ISS.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Hippocampus.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  6. "Remodeling of ryanodine receptor complex causes 'leaky' channels: a molecular mechanism for decreased exercise capacity."
    Bellinger A.M., Reiken S., Dura M., Murphy P.W., Deng S.X., Landry D.W., Nieman D., Lehnart S.E., Samaru M., LaCampagne A., Marks A.R.
    Proc. Natl. Acad. Sci. U.S.A. 105:2198-2202(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH PDE4D; PKA; RYR1 AND PROTEIN PHOSPHATASE 1.
  7. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-53, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiFKB1A_MOUSE
AccessioniPrimary (citable) accession number: P26883
Secondary accession number(s): Q545E9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.